ReDisulphID

a tool for identifying drug-targetable redox-active disulphides

Serine/threonine-protein kinase STK11

Intramolecular
Cysteine 151 and cysteine 158
Cysteine 132 and cysteine 134
A redox-regulated disulphide may form within Serine/threonine-protein kinase STK11 between cysteines 151 and 158. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
37
PDB code
2wtk
Structure name
structure of the heterotrimeric lkb1-stradalpha-mo25alpha complex
Structure deposition date
2009-09-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
54
Minimum pKa ?
10
% buried
50
Peptide accession
Q15831
Residue number A
151
Residue number B
158
Peptide name
Serine/threonine-protein kinase STK11

Ligandability

Cysteine 151 of Serine/threonine-protein kinase STK11

Cysteine 158 of Serine/threonine-protein kinase STK11

A redox-regulated disulphide may form within Serine/threonine-protein kinase STK11 between cysteines 132 and 134. However, the redox score of this cysteine pair is lower than any known redox-active intermolecular disulphide. ?

Details

Redox score ?
28
PDB code
2wtk
Structure name
structure of the heterotrimeric lkb1-stradalpha-mo25alpha complex
Structure deposition date
2009-09-16
Thiol separation (Å)
10
Half-sphere exposure sum ?
77
Minimum pKa ?
12
% buried
81
Peptide accession
Q15831
Residue number A
132
Residue number B
134
Peptide name
Serine/threonine-protein kinase STK11

Ligandability

Cysteine 132 of Serine/threonine-protein kinase STK11

Cysteine 134 of Serine/threonine-protein kinase STK11

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